We have constructed (and continue to develop) a unique laser-based facility for time-resolved fluorescence spectroscopy of biomolecules. This facility provides rapid collection and analysis of luminescence data related to macromolecular size, flexibility, folding and structural fluctuations. Our fluorescence facility was used to study the folding pattern and motions of several important proteins. We were especially interested in proteins that act as "switches" or boosters for the DNA copying processes that creates working blueprints (m-RNA) for protein construction. One such "booster", the transactivator VP16, was found to be a loose, floppy structure until it sticks to the copying machinery (TBP). Once bound, it "freezes" into the shape needed to turn up the speed of the system. This year, we also helped two different research groups develop rapid assays for the enzyme HIV integrase. This is the enzyme used by the virus that causes AIDS to paste itself into human DNA - a step that allows it to hide from immune system destruction. Two rapid, fluorescence-based assays were developed. Thus, the effectiveness of a huge variety of anti-AIDS drugs could be screened by watching changes in brightness. This year, we also developed laser methods for collecting time-resolved fluorescence spectra more rapidly and computational methods that imitate evolution in their quest to model our data. We split our efforts between immediate applications of the instruments we've already built and the development of new instruments that will give us better insight into how proteins and DNA work.